5HRD

The crystal structure of AsfvPolX:DNA2 binary complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003887	molecular_function	DNA-directed DNA polymerase activity
A	0006281	biological_process	DNA repair
A	0006974	biological_process	DNA damage response
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0034061	molecular_function	DNA polymerase activity
A	0046872	molecular_function	metal ion binding
A	0071897	biological_process	DNA biosynthetic process
B	0003677	molecular_function	DNA binding
B	0003887	molecular_function	DNA-directed DNA polymerase activity
B	0006281	biological_process	DNA repair
B	0006974	biological_process	DNA damage response
B	0016740	molecular_function	transferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
B	0034061	molecular_function	DNA polymerase activity
B	0046872	molecular_function	metal ion binding
B	0071897	biological_process	DNA biosynthetic process
C	0003677	molecular_function	DNA binding
C	0003887	molecular_function	DNA-directed DNA polymerase activity
C	0006281	biological_process	DNA repair
C	0006974	biological_process	DNA damage response
C	0016740	molecular_function	transferase activity
C	0016779	molecular_function	nucleotidyltransferase activity
C	0034061	molecular_function	DNA polymerase activity
C	0046872	molecular_function	metal ion binding
C	0071897	biological_process	DNA biosynthetic process
D	0003677	molecular_function	DNA binding
D	0003887	molecular_function	DNA-directed DNA polymerase activity
D	0006281	biological_process	DNA repair
D	0006974	biological_process	DNA damage response
D	0016740	molecular_function	transferase activity
D	0016779	molecular_function	nucleotidyltransferase activity
D	0034061	molecular_function	DNA polymerase activity
D	0046872	molecular_function	metal ion binding
D	0071897	biological_process	DNA biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue SO4 A 201

Chain	Residue
A	ARG125
A	PHE165
A	THR166
A	ARG168
A	HOH306

---

site_id	AC2
Number of Residues	3
Details	binding site for residue SO4 A 202

Chain	Residue
A	TYR22
A	LYS63
A	HIS64

---

site_id	AC3
Number of Residues	5
Details	binding site for residue SO4 B 201

Chain	Residue
B	PHE165
B	THR166
B	ARG168
B	HOH302
B	ARG125

---

site_id	AC4
Number of Residues	5
Details	binding site for residue SO4 C 201

Chain	Residue
C	ARG125
C	PHE165
C	THR166
C	ARG168
C	HOH304

---

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 D 201

Chain	Residue
D	ARG125
D	PHE165
D	THR166
D	ARG168
D	HOH308

---

site_id	AC6
Number of Residues	5
Details	binding site for residue SO4 D 202

Chain	Residue
D	TYR22
D	ASN23
D	LYS60
D	LYS63
D	HIS64

---

Functional Information from PROSITE/UniProt

site_id	PS00522
Number of Residues	20
Details	DNA_POLYMERASE_X DNA polymerase family X signature. GSLrREekmLnDVDLLIivP

Chain	Residue	Details
A	GLY38-PRO57

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI3
Number of Residues	36
Details	Region: {"description":"Involved in ssDNA binding","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11685239","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28245220","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Stabilizes dGTP in a syn conformation to overcome the Watson-Crick base pairing constraint","evidences":[{"source":"PubMed","id":"24617852","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---